Free-Solvent Model of Osmotic Pressure Revisited: Application to Concentrated IgG Solution under Physiological Conditions
The osmotic pressure measurements of bovine immuno-gamma globulin in phosphate-buffered solution at pH 7.4 and 0.13 M total salt concentration were extended to near saturation concentrations for ambient temperature. The osmotic pressure at the highest measured concentration of 424 g/L was 4.18 psi (28.3 kPa). A free-solvent model, considering solute-solvent interaction in the concentration variable, provided an excellent fit to observed osmotic pressure nonideality at even the highest protein concentration. The calculated mass of hydrated solvent compared with amounts determined from water-17O magnetic resonance for other globular proteins. This model provides an improved correlation to the data over virial equations (truncated to the third term) when only solute-solute interactions are considered. The use of mole fraction as the composition variable was critical in obtaining the excellent fit of the free-solvent model. A combination of the free-solvent correction for the concentration variable coupled with models incorporating solute-solute interaction, such as a virial expansion, will be necessary to generally describe the osmotic pressure of protein solutions for all concentrations. Copyright 1998 Academic Press. Copyright 1998Academic Press
Yousef
MA
The Department of Chemical and Biochemical Engineering, The University of Iowa, Iowa City, Iowa, 52242
Datta
R
Rodgers
VGJ